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May 14, 1996Proceedings of the National Academy of SciencesOpen Access

Functional interaction and colocalization of the herpes simplex virus 1 major regulatory protein ICP4 with EAP, a nucleolar-ribosomal protein.

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Authors

RLRosario LeopardiKarolinska Institutet BRB RoizmanUniversity of Chicago

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Implication

EAP-ICP4 interaction may modulate HSV gene expression; leaves open its role in viral replication or latency.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Leopardi et al. (1996) studied this question.

synapsesocial.com/papers/6a871e2fed1c9801b3cfa041 https://doi.org/10.1073/pnas.93.10.4572

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Protein-protein interactions: methods for detection and analysis1995 · 849 citations
2The cellular RNA-binding protein EAP recognizes a conserved stem-loop in the Epstein-Barr virus small RNA EBER 1.1993 · 46 citations
3Repression of the herpes simplex virus 1 alpha 4 gene by its gene product occurs within the context of the viral genome and is associated with all three identified cognate sites.1993 · 61 citations
4Two small RNAs encoded by Epstein-Barr virus and complexed with protein are precipitated by antibodies from patients with systemic lupus erythematosus.1981 · 588 citations
5Relationship between TATA-binding protein and herpes simplex virus type 1 ICP4 DNA-binding sites in complex formation and repression of transcription1995 · 52 citations